Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease D (Q0BVP4)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease D (Q0BVP4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0BVP4
- Type
- protein
- Length
- 395 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xDf921891Aa1d2eaE579c7ab7a9c178c8fb3840ec
- Molecule
- Ribonuclease D
- UniProt
- Q0BVP4
- Pockets
- 5 · best druggability 0.62
Structure
1 distinct chain · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease D | protein | 395 | 52% helix, 11% strand | Q0BVP4 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 286 | 0.62 | 0.80 | 27 | empty |
| 2 | 146 | 0.42 | 0.74 | 20 | empty |
| 3 | 79 | 0.32 | 0.74 | 18 | empty |
| 4 | 76 | 0.30 | 0.73 | 19 | empty |
| 5 | 60 | 0.27 | 0.73 | 12 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q0BVP4
- Elsewhere: UniProt Q0BVP4 · AlphaFold DB Q0BVP4
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